About: Pyrrolysyl-tRNA synthetase variants reveal ancestral aminoacylation function

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scientific article published on 28 August 2013

Attributes	Values
rdf:type	Item
description	videnskabelig artikel (da) article científic (ca) articolo scientifico (it) artigo científico (pt) bilimsel makale (tr) vedecký článok (sk) vetenskaplig artikel (sv) vědecký článek (cs) wetenschappelijk artikel (nl) wissenschaftlicher Artikel (de) научни чланак (sr) article scientifique (fr) artículu científicu espublizáu en 2013 (ast) наукова стаття, опублікована в серпні 2013 (uk) scientific article published on 28 August 2013 (en) مقالة علمية نشرت في 28 أغسطس 2013 (ar)
publication date	wds:Q37185389-993F0ECD-EBB9-4868-99BB-83C74C76EEB8
publication date	2013-08-28 00:00:00Z (xsd:dateTime)
language of work or name	wds:Q37185389-4A17F9D5-2D5E-4A8C-850C-35CE49E89930
language of work or name	English
cites work	wds:Q37185389-02B3182E-F0E3-423D-AB6A-5CC66DEDBF94 wds:Q37185389-0E37F63D-B7D0-4FBD-88B8-533B889F8C65 wds:Q37185389-11841B0A-BA8A-46AB-B872-676DAD91E75C wds:Q37185389-27ADA892-609E-4838-89B9-FCE6098596FB wds:Q37185389-29BF688E-E37F-457D-80C9-B20B23D0D6B2 wds:Q37185389-3C7FCF41-F0AD-4198-9163-338280473C77 wds:Q37185389-3DF81FB6-66B6-4463-8815-62FF712B7B44 wds:Q37185389-4C2B5EB7-CA4E-41A1-BA68-C5D27781A9A7 wds:Q37185389-528978ED-1B3F-44F3-A0A9-74EF950797DD wds:Q37185389-606D95F7-D01E-45D4-98C8-4CD09B295566 wds:Q37185389-797BE82A-D552-471D-9189-3D8638F2EE68 wds:Q37185389-81385FD4-032A-40D1-9255-2DB785A10A05 wds:Q37185389-814582CC-8462-466B-ABFB-99618510EFE3 wds:Q37185389-ACA859FA-3C52-4396-89AB-CBBD8A5CCC5A wds:Q37185389-B869C213-0466-437B-A675-FD2ADCF41967 wds:Q37185389-CB9C35BC-52DA-46B0-9C0A-54B4DA08BF0C wds:Q37185389-CF5A8F2D-E471-4005-83C7-E7A52892BDB8 wds:Q37185389-D77D147F-454C-494C-87E8-9C462D0CF9DD wds:Q37185389-DAD48CD8-D376-45C3-855A-CDB95016D81A wds:Q37185389-E67B72B8-3765-466F-88A7-C69B90C5011F
cites work	PHENIX: a comprehensive Python-based system for macromolecular structure solution Structure of pyrrolysyl-tRNA synthetase, an archaeal enzyme for genetic code innovation Crystallographic studies on multiple conformational states of active-site loops in pyrrolysyl-tRNA synthetase Stereochemical Basis for Engineered Pyrrolysyl-tRNA Synthetase and the Efficient in Vivo Incorporation of Structurally Divergent Non-native Amino Acids Substrate specificity is determined by amino acid binding pocket size in Escherichia coli phenylalanyl-tRNA synthetase. Specificity of pyrrolysyl-tRNA synthetase for pyrrolysine and pyrrolysine analogs Designer proteins: applications of genetic code expansion in cell biology Engineering and characterization of a superfolder green fluorescent protein Idiosyncrasy and identity in the prokaryotic phe-system: Crystal structure ofE. coliphenylalanyl-tRNA synthetase complexed with phenylalanine and AMP Recent advances in genetic code engineering in Escherichia coli Functional context, biosynthesis, and genetic encoding of pyrrolysine N-acetyl lysyl-tRNA synthetases evolved by a CcdB-based selection possess N-acetyl lysine specificity in vitro and in vivo A rationally designed pyrrolysyl-tRNA synthetase mutant with a broad substrate spectrum Genetic incorporation of twelve meta-substituted phenylalanine derivatives using a single pyrrolysyl-tRNA synthetase mutant Synthesis of proteins with defined posttranslational modifications using the genetic noncanonical amino acid incorporation approach. A facile system for genetic incorporation of two different noncanonical amino acids into one protein in Escherichia coli. The de novo engineering of pyrrolysyl-tRNA synthetase for genetic incorporation of L-phenylalanine and its derivatives. Distinct genetic code expansion strategies for selenocysteine and pyrrolysine are reflected in different aminoacyl-tRNA formation systems. Recognition of pyrrolysine tRNA by the Desulfitobacterium hafniense pyrrolysyl-tRNA synthetase Prokaryotic and eukaryotic tetrameric phenylalanyl-tRNA synthetases display conservation of the binding mode of the tRNA(Phe) CCA end.
author name string	wds:Q37185389-3B103A05-C920-4833-B277-A251FE61613C wds:Q37185389-82D9F809-0B3F-4E50-A8BF-9119BBD9B9A5 wds:Q37185389-A5E6045F-AFD0-4994-9E1F-1EC6DFAAA7E3 wds:Q37185389-B34DAC58-29C4-4B51-BABE-ABD554BBB98D
author name string	Dieter Söll Li-Tao Guo Takuya Umehara Jae-hyeong Ko
rdfs:label	Pyrrolysyl-tRNA synthetase variants reveal ancestral aminoacylation function. (nl) Pyrrolysyl-tRNA synthetase variants reveal ancestral aminoacylation function (en) Pyrrolysyl-tRNA synthetase variants reveal ancestral aminoacylation function (ast)
skos:prefLabel	Pyrrolysyl-tRNA synthetase variants reveal ancestral aminoacylation function. (nl) Pyrrolysyl-tRNA synthetase variants reveal ancestral aminoacylation function (en) Pyrrolysyl-tRNA synthetase variants reveal ancestral aminoacylation function (ast)
name	Pyrrolysyl-tRNA synthetase variants reveal ancestral aminoacylation function. (nl) Pyrrolysyl-tRNA synthetase variants reveal ancestral aminoacylation function (en) Pyrrolysyl-tRNA synthetase variants reveal ancestral aminoacylation function (ast)
author	wds:Q37185389-4B9026A8-67EF-4305-BB9D-0180E7221691 wds:Q37185389-BA85B0E1-586B-4A67-B5F2-BF7B29D5DADD
author	Akiyoshi Nakamura Yane-Shih Wang
title	wds:Q37185389-4756AAE9-85F5-4EF9-9AC7-AA3FD035212D
title	Pyrrolysyl-tRNA synthetase variants reveal ancestral aminoacylation function (en)
page(s)	wds:Q37185389-21E5B6A5-A9E0-4966-B99B-F2EC87291728
page(s)	3243-3248
instance of	wds:Q37185389-15CC3C67-0FB0-4F80-B90A-5CC4861FF726
instance of	scholarly article
PubMed ID	wds:Q37185389-A34C50AD-1F29-42C4-A65F-4BD5AC4A6CE5
PubMed ID	http://rdf.ncbi.nlm.nih.gov/pubchem/reference/23994531
PubMed ID	23994531
published in	wds:Q37185389-ED63C116-94F4-4579-9E67-B31DD55FCEEA
published in	FEBS Letters
issue	wds:Q37185389-404B5B26-4858-4EEC-88CE-8702976A1DE5
volume	wds:Q37185389-A707AB4B-C8A5-4AC7-BE1F-00CDEA1B3EA6
issue	19
volume	587
DOI	wds:Q37185389-FB7CE810-E60F-4C7B-96C3-6BC0E110550A
DOI	http://dx.doi.org/10.1016/J.FEBSLET.2013.08.018
DOI	10.1016/J.FEBSLET.2013.08.018

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